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Protein

Lysine-specific demethylase 4B

Gene

KDM4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate.1 Publication

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331Alpha-ketoglutarateBy similarity
Metal bindingi189 – 1891Iron; catalyticPROSITE-ProRule annotation
Metal bindingi191 – 1911Iron; catalyticPROSITE-ProRule annotation
Binding sitei199 – 1991Alpha-ketoglutarateBy similarity
Binding sitei207 – 2071Alpha-ketoglutarateBy similarity
Metal bindingi235 – 2351ZincBy similarity
Metal bindingi241 – 2411ZincBy similarity
Metal bindingi277 – 2771Iron; catalyticPROSITE-ProRule annotation
Metal bindingi307 – 3071ZincBy similarity
Metal bindingi309 – 3091ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri731 – 78959PHD-type 1Add
BLAST
Zinc fingeri851 – 90757PHD-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.14.11.B1. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 4B (EC:1.14.11.-)
Alternative name(s):
JmjC domain-containing histone demethylation protein 3B
Jumonji domain-containing protein 2B
Gene namesi
Name:KDM4B
Synonyms:JHDM3B, JMJD2B, KIAA0876
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:29136. KDM4B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164721452.

Chemistry

ChEMBLiCHEMBL3313832.

Polymorphism and mutation databases

BioMutaiKDM4B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10961096Lysine-specific demethylase 4BPRO_0000183175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei566 – 5661PhosphoserineCombined sources
Modified residuei602 – 6021N6-acetyllysineCombined sources
Modified residuei1065 – 10651PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO94953.
MaxQBiO94953.
PaxDbiO94953.
PeptideAtlasiO94953.
PRIDEiO94953.

PTM databases

iPTMnetiO94953.
PhosphoSiteiO94953.

Expressioni

Gene expression databases

BgeeiO94953.
CleanExiHS_JMJD2B.
ExpressionAtlasiO94953. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi116669. 28 interactions.
DIPiDIP-47283N.
IntActiO94953. 6 interactions.
MINTiMINT-1427202.
STRINGi9606.ENSP00000159111.

Structurei

Secondary structure

1
1096
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 254Combined sources
Helixi28 – 3710Combined sources
Helixi40 – 434Combined sources
Beta strandi44 – 485Combined sources
Helixi63 – 653Combined sources
Beta strandi67 – 704Combined sources
Beta strandi72 – 798Combined sources
Beta strandi82 – 898Combined sources
Helixi95 – 1039Combined sources
Turni105 – 1073Combined sources
Helixi115 – 12511Combined sources
Beta strandi132 – 1387Combined sources
Helixi157 – 1593Combined sources
Helixi160 – 1656Combined sources
Turni170 – 1723Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi185 – 1895Combined sources
Helixi192 – 1943Combined sources
Beta strandi196 – 20510Combined sources
Beta strandi207 – 2126Combined sources
Helixi214 – 2163Combined sources
Helixi217 – 22711Combined sources
Helixi229 – 2346Combined sources
Helixi238 – 2414Combined sources
Beta strandi244 – 2463Combined sources
Helixi248 – 2536Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi283 – 29210Combined sources
Helixi295 – 2973Combined sources
Helixi298 – 3036Combined sources
Helixi319 – 3257Combined sources
Helixi327 – 3348Combined sources
Beta strandi924 – 9285Combined sources
Beta strandi934 – 95118Combined sources
Beta strandi957 – 9615Combined sources
Helixi963 – 9653Combined sources
Beta strandi966 – 9694Combined sources
Helixi971 – 9744Combined sources
Beta strandi982 – 9865Combined sources
Beta strandi992 – 101019Combined sources
Beta strandi1015 – 10195Combined sources
Helixi1020 – 10223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LXLX-ray1.87A1-348[»]
4UC4X-ray2.56A/B917-1031[»]
ProteinModelPortaliO94953.
SMRiO94953. Positions 9-337, 917-1034.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 5743JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini146 – 309164JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini917 – 97458Tudor 1Add
BLAST
Domaini975 – 103157Tudor 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi463 – 53573Pro-richAdd
BLAST

Domaini

The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity).By similarity

Sequence similaritiesi

Belongs to the JHDM3 histone demethylase family.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.Curated
Contains 2 Tudor domains.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri731 – 78959PHD-type 1Add
BLAST
Zinc fingeri851 – 90757PHD-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
InParanoidiO94953.
KOiK06709.
OrthoDBiEOG7TQV03.
PhylomeDBiO94953.
TreeFamiTF106449.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94953-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSEDHGAQN PSCKIMTFRP TMEEFKDFNK YVAYIESQGA HRAGLAKIIP
60 70 80 90 100
PKEWKPRQTY DDIDDVVIPA PIQQVVTGQS GLFTQYNIQK KAMTVGEYRR
110 120 130 140 150
LANSEKYCTP RHQDFDDLER KYWKNLTFVS PIYGADISGS LYDDDVAQWN
160 170 180 190 200
IGSLRTILDM VERECGTIIE GVNTPYLYFG MWKTTFAWHT EDMDLYSINY
210 220 230 240 250
LHFGEPKSWY AIPPEHGKRL ERLAIGFFPG SSQGCDAFLR HKMTLISPII
260 270 280 290 300
LKKYGIPFSR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY
310 320 330 340 350
GKVATQCTCR KDMVKISMDV FVRILQPERY ELWKQGKDLT VLDHTRPTAL
360 370 380 390 400
TSPELSSWSA SRASLKAKLL RRSHRKRSQP KKPKPEDPKF PGEGTAGAAL
410 420 430 440 450
LEEAGGSVKE EAGPEVDPEE EEEEPQPLPH GREAEGAEED GRGKLRPTKA
460 470 480 490 500
KSERKKKSFG LLPPQLPPPP AHFPSEEALW LPSPLEPPVL GPGPAAMEES
510 520 530 540 550
PLPAPLNVVP PEVPSEELEA KPRPIIPMLY VVPRPGKAAF NQEHVSCQQA
560 570 580 590 600
FEHFAQKGPT WKEPVSPMEL TGPEDGAASS GAGRMETKAR AGEGQAPSTF
610 620 630 640 650
SKLKMEIKKS RRHPLGRPPT RSPLSVVKQE ASSDEEASPF SGEEDVSDPD
660 670 680 690 700
ALRPLLSLQW KNRAASFQAE RKFNAAAART EPYCAICTLF YPYCQALQTE
710 720 730 740 750
KEAPIASLGK GCPATLPSKS RQKTRPLIPE MCFTSGGENT EPLPANSYIG
760 770 780 790 800
DDGTSPLIAC GKCCLQVHAS CYGIRPELVN EGWTCSRCAA HAWTAECCLC
810 820 830 840 850
NLRGGALQMT TDRRWIHVIC AIAVPEARFL NVIERHPVDI SAIPEQRWKL
860 870 880 890 900
KCVYCRKRMK KVSGACIQCS YEHCSTSFHV TCAHAAGVLM EPDDWPYVVS
910 920 930 940 950
ITCLKHKSGG HAVQLLRAVS LGQVVITKNR NGLYYRCRVI GAASQTCYEV
960 970 980 990 1000
NFDDGSYSDN LYPESITSRD CVQLGPPSEG ELVELRWTDG NLYKAKFISS
1010 1020 1030 1040 1050
VTSHIYQVEF EDGSQLTVKR GDIFTLEEEL PKRVRSRLSL STGAPQEPAF
1060 1070 1080 1090
SGEEAKAAKR PRVGTPLATE DSGRSQDYVA FVESLLQVQG RPGAPF
Length:1,096
Mass (Da):121,897
Last modified:March 20, 2007 - v4
Checksum:i300D5CD6F2DD4330
GO
Isoform 2 (identifier: O94953-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-448: SHRKRSQPKK...EDGRGKLRPT → TPPCVSPHRP...LRMATQDPCR
     449-1096: Missing.

Note: No experimental confirmation available.
Show »
Length:448
Mass (Da):50,582
Checksum:i84E9B0DEEF9C84F9
GO

Sequence cautioni

The sequence AAC33799.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA74899.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291N → T.
Corresponds to variant rs11667206 [ dbSNP | Ensembl ].
VAR_026223
Natural varianti710 – 7101K → E.4 Publications
Corresponds to variant rs2620836 [ dbSNP | Ensembl ].
VAR_026224

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei373 – 44876SHRKR…KLRPT → TPPCVSPHRPSQPGIWCPPG GEAKASAASWLLTTRGHGDT EAGPGLGGDPLHAQSEGQAS CVSTSRLRMATQDPCR in isoform 2. 1 PublicationVSP_018307Add
BLAST
Alternative sequencei449 – 1096648Missing in isoform 2. 1 PublicationVSP_018308Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020683 mRNA. Translation: BAA74899.2. Different initiation.
AC005595 Genomic DNA. Translation: AAC33799.1. Sequence problems.
AC022517 Genomic DNA. Translation: AAF31271.1.
CH471139 Genomic DNA. Translation: EAW69181.1.
CH471139 Genomic DNA. Translation: EAW69183.1.
BC063889 mRNA. Translation: AAH63889.1.
BC136611 mRNA. Translation: AAI36612.1.
AL133622 mRNA. Translation: CAB63748.2.
CCDSiCCDS12138.1. [O94953-1]
PIRiT43460.
RefSeqiNP_055830.1. NM_015015.2.
UniGeneiHs.654816.

Genome annotation databases

EnsembliENST00000381759; ENSP00000371178; ENSG00000127663. [O94953-2]
GeneIDi23030.
KEGGihsa:23030.
UCSCiuc002mbq.5. human. [O94953-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020683 mRNA. Translation: BAA74899.2. Different initiation.
AC005595 Genomic DNA. Translation: AAC33799.1. Sequence problems.
AC022517 Genomic DNA. Translation: AAF31271.1.
CH471139 Genomic DNA. Translation: EAW69181.1.
CH471139 Genomic DNA. Translation: EAW69183.1.
BC063889 mRNA. Translation: AAH63889.1.
BC136611 mRNA. Translation: AAI36612.1.
AL133622 mRNA. Translation: CAB63748.2.
CCDSiCCDS12138.1. [O94953-1]
PIRiT43460.
RefSeqiNP_055830.1. NM_015015.2.
UniGeneiHs.654816.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LXLX-ray1.87A1-348[»]
4UC4X-ray2.56A/B917-1031[»]
ProteinModelPortaliO94953.
SMRiO94953. Positions 9-337, 917-1034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116669. 28 interactions.
DIPiDIP-47283N.
IntActiO94953. 6 interactions.
MINTiMINT-1427202.
STRINGi9606.ENSP00000159111.

Chemistry

ChEMBLiCHEMBL3313832.

PTM databases

iPTMnetiO94953.
PhosphoSiteiO94953.

Polymorphism and mutation databases

BioMutaiKDM4B.

Proteomic databases

EPDiO94953.
MaxQBiO94953.
PaxDbiO94953.
PeptideAtlasiO94953.
PRIDEiO94953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381759; ENSP00000371178; ENSG00000127663. [O94953-2]
GeneIDi23030.
KEGGihsa:23030.
UCSCiuc002mbq.5. human. [O94953-1]

Organism-specific databases

CTDi23030.
GeneCardsiKDM4B.
HGNCiHGNC:29136. KDM4B.
MIMi609765. gene.
neXtProtiNX_O94953.
PharmGKBiPA164721452.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
InParanoidiO94953.
KOiK06709.
OrthoDBiEOG7TQV03.
PhylomeDBiO94953.
TreeFamiTF106449.

Enzyme and pathway databases

BRENDAi1.14.11.B1. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Miscellaneous databases

ChiTaRSiKDM4B. human.
GeneWikiiJMJD2B.
GenomeRNAii23030.
PROiO94953.
SOURCEiSearch...

Gene expression databases

BgeeiO94953.
CleanExiHS_JMJD2B.
ExpressionAtlasiO94953. baseline and differential.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-710.
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-710.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT GLU-710.
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1096, VARIANT GLU-710.
    Tissue: Testis.
  7. "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
    Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
    J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases."
    Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.
    Cell 125:467-481(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND THR-1065, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND THR-1065, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKDM4B_HUMAN
AccessioniPrimary (citable) accession number: O94953
Secondary accession number(s): B9EGN8
, D6W631, O75274, Q6P3R5, Q9P1V1, Q9UF40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 20, 2007
Last modified: July 6, 2016
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.